ID   MURA_ECOLI              Reviewed;         419 AA.
AC   P0A749; P28909; Q2M923;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   24-JAN-2024, entry version 154.
DE   RecName: Full=UDP-N-acetylglucosamine 1-carboxyvinyltransferase {ECO:0000255|HAMAP-Rule:MF_00111};
DE            EC=2.5.1.7 {ECO:0000255|HAMAP-Rule:MF_00111};
DE   AltName: Full=Enoylpyruvate transferase {ECO:0000255|HAMAP-Rule:MF_00111};
DE   AltName: Full=UDP-N-acetylglucosamine enolpyruvyl transferase {ECO:0000255|HAMAP-Rule:MF_00111};
DE            Short=EPT {ECO:0000255|HAMAP-Rule:MF_00111};
GN   Name=murA {ECO:0000255|HAMAP-Rule:MF_00111}; Synonyms=murZ;
GN   OrderedLocusNames=b3189, JW3156;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, FUNCTION,
RP   CATALYTIC ACTIVITY, AND PATHWAY.
RC   STRAIN=K12 / AB1157;
RX   PubMed=1512209; DOI=10.1128/jb.174.17.5748-5752.1992;
RA   Marquardt J.L., Siegele D.A., Kolter R., Walsh C.T.;
RT   "Cloning and sequencing of Escherichia coli murZ and purification of its
RT   product, a UDP-N-acetylglucosamine enolpyruvyl transferase.";
RL   J. Bacteriol. 174:5748-5752(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=O26 / NGY47;
RX   PubMed=10103182; DOI=10.1128/aac.43.4.789;
RA   Horii T., Kimura T., Sato K., Shibayama K., Ohta M.;
RT   "Emergence of fosfomycin-resistant isolates of Shiga-like toxin-producing
RT   Escherichia coli O26.";
RL   Antimicrob. Agents Chemother. 43:789-793(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=21445328; DOI=10.1371/journal.pbio.1001033;
RA   Mutschler H., Gebhardt M., Shoeman R.L., Meinhart A.;
RT   "A novel mechanism of programmed cell death in bacteria by toxin-antitoxin
RT   systems corrupts peptidoglycan synthesis.";
RL   PLoS Biol. 9:E1001033-E1001033(2011).
RN   [6] {ECO:0007744|PDB:1UAE}
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH
RP   UDP-N-ACETYLGLUCOSAMINE AND FOSFOMYCIN, AND ACTIVE SITE.
RX   PubMed=8994972; DOI=10.1016/s0969-2126(96)00153-0;
RA   Skarzynski T., Mistry A., Wonacott A., Hutchinson S.E., Kelly V.A.,
RA   Duncan K.;
RT   "Structure of UDP-N-acetylglucosamine enolpyruvyl transferase, an enzyme
RT   essential for the synthesis of bacterial peptidoglycan, complexed with
RT   substrate UDP-N-acetylglucosamine and the drug fosfomycin.";
RL   Structure 4:1465-1474(1996).
RN   [7] {ECO:0007744|PDB:1A2N}
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH FLUORINATED ANALOG OF
RP   THE REACTION TETRAHEDRAL INTERMEDIATE.
RX   PubMed=9485407; DOI=10.1021/bi9722608;
RA   Skarzynski T., Kim D.H., Lees W.J., Walsh C.T., Duncan K.;
RT   "Stereochemical course of enzymatic enolpyruvyl transfer and catalytic
RT   conformation of the active site revealed by the crystal structure of the
RT   fluorinated analogue of the reaction tetrahedral intermediate bound to the
RT   active site of the C115A mutant of MurA.";
RL   Biochemistry 37:2572-2577(1998).
RN   [8] {ECO:0007744|PDB:3KQJ, ECO:0007744|PDB:3KR6}
RP   X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH
RP   UDP-N-ACETYLGLUCOSAMINE AND FOSFOMYCIN, FUNCTION, CATALYTIC ACTIVITY,
RP   ACTIVITY REGULATION, AND ACTIVE SITE.
RX   PubMed=20392080; DOI=10.1021/bi100365b;
RA   Han H., Yang Y., Olesen S.H., Becker A., Betzi S., Schoenbrunn E.;
RT   "The fungal product terreic acid is a covalent inhibitor of the bacterial
RT   cell wall biosynthetic enzyme UDP-N-acetylglucosamine 1-
RT   carboxyvinyltransferase (MurA).";
RL   Biochemistry 49:4276-4282(2010).
RN   [9] {ECO:0007744|PDB:3SWD}
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-418 IN COMPLEX WITH SUBSTRATE
RP   ANALOG, ACTIVE SITE, AND FORMATION OF COVALENT REACTION INTERMEDIATE.
RX   PubMed=22378791; DOI=10.1074/jbc.m112.342725;
RA   Zhu J.Y., Yang Y., Han H., Betzi S., Olesen S.H., Marsilio F.,
RA   Schoenbrunn E.;
RT   "Functional consequence of covalent reaction of phosphoenolpyruvate with
RT   UDP-N-acetylglucosamine 1-carboxyvinyltransferase (MurA).";
RL   J. Biol. Chem. 287:12657-12667(2012).
CC   -!- FUNCTION: Cell wall formation (PubMed:1512209). Adds enolpyruvyl to
CC       UDP-N-acetylglucosamine (PubMed:1512209, PubMed:20392080). Target for
CC       the antibiotic fosfomycin. {ECO:0000269|PubMed:1512209,
CC       ECO:0000269|PubMed:20392080}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine =
CC         phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine;
CC         Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705,
CC         ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00111,
CC         ECO:0000269|PubMed:1512209, ECO:0000269|PubMed:20392080};
CC   -!- ACTIVITY REGULATION: Competitively inhibited by UDP-N-acetylglucosamine
CC       3'-phosphate, with a Ki of 7 uM (PubMed:21445328). In vitro inhibited
CC       by covalent binding of fosfomycin and the fungal product terreic acid
CC       in the presence of substrate UDP-N-acetylglucosamine, with an
CC       inactivation rate constant of 102 M(-1)sec(-1) for terreic acid
CC       (PubMed:20392080). {ECO:0000269|PubMed:20392080,
CC       ECO:0000269|PubMed:21445328}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=15 uM for UDP-N-acetylglucosamine {ECO:0000269|PubMed:21445328};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00111, ECO:0000269|PubMed:1512209}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00111,
CC       ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the EPSP synthase family. MurA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00111}.
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DR   EMBL; M92358; AAA24187.1; -; Genomic_DNA.
DR   EMBL; U18997; AAA57990.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76221.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77233.1; -; Genomic_DNA.
DR   EMBL; AB028039; BAA78107.1; -; Genomic_DNA.
DR   PIR; A44917; A44917.
DR   RefSeq; NP_417656.1; NC_000913.3.
DR   RefSeq; WP_000357259.1; NZ_STEB01000012.1.
DR   PDB; 1A2N; X-ray; 2.80 A; A=1-419.
DR   PDB; 1UAE; X-ray; 1.80 A; A=1-419.
DR   PDB; 2Z2C; X-ray; 2.05 A; A/B/C/D=1-419.
DR   PDB; 3ISS; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=1-418.
DR   PDB; 3KQJ; X-ray; 1.70 A; A=1-419.
DR   PDB; 3KR6; X-ray; 1.70 A; A=1-419.
DR   PDB; 3SWD; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=1-418.
DR   PDB; 5VM7; EM; 5.70 A; B=1-419.
DR   PDBsum; 1A2N; -.
DR   PDBsum; 1UAE; -.
DR   PDBsum; 2Z2C; -.
DR   PDBsum; 3ISS; -.
DR   PDBsum; 3KQJ; -.
DR   PDBsum; 3KR6; -.
DR   PDBsum; 3SWD; -.
DR   PDBsum; 5VM7; -.
DR   AlphaFoldDB; P0A749; -.
DR   SMR; P0A749; -.
DR   BioGRID; 4262438; 644.
DR   BioGRID; 852016; 3.
DR   DIP; DIP-48060N; -.
DR   IntAct; P0A749; 25.
DR   STRING; 511145.b3189; -.
DR   BindingDB; P0A749; -.
DR   ChEMBL; CHEMBL1984; -.
DR   DrugBank; DB00828; Fosfomycin.
DR   DrugCentral; P0A749; -.
DR   jPOST; P0A749; -.
DR   PaxDb; 511145-b3189; -.
DR   EnsemblBacteria; AAC76221; AAC76221; b3189.
DR   GeneID; 75173363; -.
DR   GeneID; 947703; -.
DR   KEGG; ecj:JW3156; -.
DR   KEGG; eco:b3189; -.
DR   PATRIC; fig|1411691.4.peg.3542; -.
DR   EchoBASE; EB1333; -.
DR   eggNOG; COG0766; Bacteria.
DR   HOGENOM; CLU_027387_0_0_6; -.
DR   InParanoid; P0A749; -.
DR   OMA; CDPHRAT; -.
DR   PhylomeDB; P0A749; -.
DR   BioCyc; EcoCyc:UDPNACETYLGLUCOSAMENOLPYRTRANS-MONOMER; -.
DR   BioCyc; MetaCyc:UDPNACETYLGLUCOSAMENOLPYRTRANS-MONOMER; -.
DR   BRENDA; 2.5.1.7; 2026.
DR   SABIO-RK; P0A749; -.
DR   UniPathway; UPA00219; -.
DR   EvolutionaryTrace; P0A749; -.
DR   PRO; PR:P0A749; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0008760; F:UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity; IDA:EcoCyc.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IMP:EcoCyc.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   GO; GO:0019277; P:UDP-N-acetylgalactosamine biosynthetic process; IEA:InterPro.
DR   CDD; cd01555; UdpNAET; 1.
DR   Gene3D; 3.65.10.10; Enolpyruvate transferase domain; 2.
DR   HAMAP; MF_00111; MurA; 1.
DR   InterPro; IPR001986; Enolpyruvate_Tfrase_dom.
DR   InterPro; IPR036968; Enolpyruvate_Tfrase_sf.
DR   InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
DR   InterPro; IPR005750; UDP_GlcNAc_COvinyl_MurA.
DR   NCBIfam; TIGR01072; murA; 1.
DR   PANTHER; PTHR43783; UDP-N-ACETYLGLUCOSAMINE 1-CARBOXYVINYLTRANSFERASE; 1.
DR   PANTHER; PTHR43783:SF1; UDP-N-ACETYLGLUCOSAMINE 1-CARBOXYVINYLTRANSFERASE; 1.
DR   Pfam; PF00275; EPSP_synthase; 1.
DR   SUPFAM; SSF55205; EPT/RTPC-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Cell shape;
KW   Cell wall biogenesis/degradation; Cytoplasm; Direct protein sequencing;
KW   Peptidoglycan synthesis; Pyruvate; Reference proteome; Transferase.
FT   CHAIN           1..419
FT                   /note="UDP-N-acetylglucosamine 1-carboxyvinyltransferase"
FT                   /id="PRO_0000178870"
FT   ACT_SITE        115
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000269|PubMed:20392080,
FT                   ECO:0000269|PubMed:8994972, ECO:0000305|PubMed:22378791,
FT                   ECO:0007744|PDB:1UAE, ECO:0007744|PDB:3KR6"
FT   BINDING         22..23
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000305|PubMed:20392080,
FT                   ECO:0000305|PubMed:22378791, ECO:0007744|PDB:3KR6,
FT                   ECO:0007744|PDB:3SWD"
FT   BINDING         91
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000269|PubMed:20392080,
FT                   ECO:0007744|PDB:3KR6"
FT   BINDING         120..124
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000269|PubMed:20392080,
FT                   ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3KR6"
FT   BINDING         160..163
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000269|PubMed:20392080,
FT                   ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3KR6"
FT   BINDING         305
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000269|PubMed:20392080,
FT                   ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3KR6"
FT   BINDING         327
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000269|PubMed:20392080,
FT                   ECO:0007744|PDB:3KR6"
FT   MOD_RES         115
FT                   /note="2-(S-cysteinyl)pyruvic acid O-phosphothioketal"
FT                   /evidence="ECO:0000305|PubMed:22378791"
FT   STRAND          3..8
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   STRAND          14..17
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   HELIX           22..31
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   HELIX           32..34
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   STRAND          35..37
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   STRAND          39..43
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   HELIX           48..59
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   STRAND          63..65
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   STRAND          70..73
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   HELIX           74..76
FT                   /evidence="ECO:0007829|PDB:2Z2C"
FT   HELIX           84..87
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   HELIX           92..96
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   HELIX           97..104
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   STRAND          105..110
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   STRAND          115..118
FT                   /evidence="ECO:0007829|PDB:3SWD"
FT   HELIX           123..131
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   STRAND          135..139
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   STRAND          142..146
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   STRAND          148..150
FT                   /evidence="ECO:0007829|PDB:2Z2C"
FT   STRAND          155..157
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   HELIX           163..173
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   STRAND          176..184
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   HELIX           189..200
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   STRAND          204..206
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   STRAND          210..216
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   STRAND          224..227
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   HELIX           232..245
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   STRAND          248..253
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   HELIX           256..258
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   HELIX           260..268
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   STRAND          272..275
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   STRAND          277..283
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   STRAND          293..295
FT                   /evidence="ECO:0007829|PDB:2Z2C"
FT   HELIX           304..306
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   HELIX           307..316
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   STRAND          317..324
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   STRAND          326..328
FT                   /evidence="ECO:0007829|PDB:3ISS"
FT   TURN            329..333
FT                   /evidence="ECO:0007829|PDB:2Z2C"
FT   HELIX           334..339
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   TURN            340..342
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   STRAND          344..348
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   STRAND          351..355
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   STRAND          364..366
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   HELIX           370..382
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   STRAND          383..390
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   HELIX           392..397
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   STRAND          399..401
FT                   /evidence="ECO:0007829|PDB:3ISS"
FT   HELIX           402..408
FT                   /evidence="ECO:0007829|PDB:3KQJ"
FT   STRAND          412..417
FT                   /evidence="ECO:0007829|PDB:3KQJ"
SQ   SEQUENCE   419 AA;  44818 MW;  6B75A842255E53F7 CRC64;
     MDKFRVQGPT KLQGEVTISG AKNAALPILF AALLAEEPVE IQNVPKLKDV DTSMKLLSQL
     GAKVERNGSV HIDARDVNVF CAPYDLVKTM RASIWALGPL VARFGQGQVS LPGGCTIGAR
     PVDLHISGLE QLGATIKLEE GYVKASVDGR LKGAHIVMDK VSVGATVTIM CAATLAEGTT
     IIENAAREPE IVDTANFLIT LGAKISGQGT DRIVIEGVER LGGGVYRVLP DRIETGTFLV
     AAAISRGKII CRNAQPDTLD AVLAKLRDAG ADIEVGEDWI SLDMHGKRPK AVNVRTAPHP
     AFPTDMQAQF TLLNLVAEGT GFITETVFEN RFMHVPELSR MGAHAEIESN TVICHGVEKL
     SGAQVMATDL RASASLVLAG CIAEGTTVVD RIYHIDRGYE RIEDKLRALG ANIERVKGE
//